Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/355982
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampSkaf, Munir Salomão-
dc.contributor.authorunicampStankovic, Ivana-
dc.typeArtigopt_BR
dc.titleA linker of the proline-threonine repeating motif sequence is bimodalpt_BR
dc.contributor.authorSkaf, Munir Salomão-
dc.contributor.authorPolikarpov, Igor-
dc.contributor.authorStanković, Ivana M.-
dc.subjectDinâmica molecularpt_BR
dc.subjectEndoglucanasespt_BR
dc.subject.otherlanguageMolecular dynamicspt_BR
dc.subject.otherlanguageEndoglucanasespt_BR
dc.description.abstractThe linker of the endoglucanase from Xanthomonas campestris pv. campestris ((PT)12) has a specific sequence, a repeating proline-threonine motif. In order to understand its role, it has been compared to a regular sequence linker, in this work—the cellobiohydrolase 2 from Trichoderma reesei (CBH2). Elastic properties of the two linkers have been estimated by calculating free energy profile along the linker length from an enhanced sampling molecular dynamics simulation. The (PT)12 exhibits more pronounced elastic behaviour than CBH2. The PT repeating motif results in a two-mode energy profile which could be very useful in the enzyme motions along the substrate during hydrolytic catalysispt_BR
dc.relation.ispartofJournal of molecular modelingpt_BR
dc.relation.ispartofabbreviationJ mol modelpt_BR
dc.publisher.cityHeidelbergpt_BR
dc.publisher.countryAlemanhapt_BR
dc.publisherSpringerpt_BR
dc.date.issued2020-
dc.date.monthofcirculationJunept_BR
dc.language.isoengpt_BR
dc.description.volume26pt_BR
dc.rightsFechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1610-2940pt_BR
dc.identifier.eissn0948-502326pt_BR
dc.identifier.doi10.1007/s00894-020-04434-0pt_BR
dc.identifier.urlhttps://link.springer.com/article/10.1007%2Fs00894-020-04434-0pt_BR
dc.description.sponsorshipCONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQpt_BR
dc.description.sponsorshipFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPpt_BR
dc.description.sponsordocumentnumber490022/2009-0; 550985/2010-7pt_BR
dc.description.sponsordocumentnumber08/56255-9; 09/54035-4;10/08680-2pt_BR
dc.date.available2021-02-17T15:39:08Z-
dc.date.accessioned2021-02-17T15:39:08Z-
dc.description.provenanceSubmitted by Susilene Barbosa da Silva (susilene@unicamp.br) on 2021-02-17T15:39:08Z No. of bitstreams: 0en
dc.description.provenanceMade available in DSpace on 2021-02-17T15:39:08Z (GMT). No. of bitstreams: 0 Previous issue date: 2020en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/355982-
dc.contributor.departmentDepartamento de Físico-Químicapt_BR
dc.contributor.departmentSem informaçãopt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.contributor.unidadeInstituto de Químicapt_BR
dc.subject.keywordReplica exchange molecular dynamicspt_BR
dc.subject.keywordLinkerpt_BR
dc.identifier.source000543521200001pt_BR
dc.creator.orcid0000-0001-7485-1228pt_BR
dc.creator.orcidSem informaçãopt_BR
dc.type.formArtigo originalpt_BR
dc.identifier.articleid178pt_BR
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